ArticleBiomolecules2020
The Non-Fibrillating N-Terminal of α-Synuclein Binds and Co-Fibrillates with Heparin.
Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Conformational determinants of glucagon stability and aggregation kinetics in aqueous and commercial formulations.Protein science : a publication of the Protein Society · 2026Article
- 1,1'-Bi-2,2'-naphthol-Based Macrocycles as Dual Metal Cation Chemosensors: Synthesis, Spectroscopic Characterization, and Molecular Dynamics Insights.Organic letters · 2026Article
- Structural Dynamics of GLP-1 Analogues: Folding Energetics, Lipidation-Driven Assembly, and Aggregation Mechanisms.Molecules (Basel, Switzerland) · 2026Review
- Towards a Biologically Defined Diagnosis: Incorporating Pathophysiological Measures Into Parkinson's Disease Clinical Criteria.Parkinson's disease · 2026Review
- Cell Surface Markers of Mesenchymal Stem Cells: Current Knowledge and Advances in Characterization Technologies.Life (Basel, Switzerland) · 2025Review
- The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion.Protein science : a publication of the Protein Society · 2024Article
- Monomeric α-synuclein activates the plasma membrane calcium pump.The EMBO journal · 2023Article
- Monitoring the Conformational Changes of the Aβ(25-35) Peptide in SDS Micelles: A Matter of Time.International journal of molecular sciences · 2023Article
- Neurons and Glia Interplay in α-Synucleinopathies.International journal of molecular sciences · 2021Review
- Refinement of α-Synuclein Ensembles Against SAXS Data: Comparison of Force Fields and Methods.Frontiers in molecular biosciences · 2021Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
The intrinsically disordered protein α-synuclein (aSN) is, in its fibrillated state, the main component of Lewy bodies-hallmarks of Parkinson's disease. Additional Lewy body components include glycosaminoglycans, including heparan sulfate proteoglycans. In humans, heparan sulfate has, in an age-dependent manner, shown increased levels of sulfation. Heparin, a highly sulfated glycosaminoglycan, is a relevant mimic for mature heparan sulfate and has been shown to influence aSN fibrillation. Here, we decompose the underlying properties of the interaction between heparin and aSN and the effect of heparin on fibrillation. Via the isolation of the first 61 residues of aSN, which lacked intrinsic fibrillation propensity, fibrillation could be induced by heparin, and access to the initial steps in fibrillation was possible. Here, structural changes with shifts from disorder via type I β-turns to β-sheets were revealed, correlating with an increase in the aSN
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.